Evidence map›Paper›PMID 30616824›Full record

ArticleMethods in cell biology2019

Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus on

Andrew B Kleist, Francis Peterson, Robert C Tyler, Martin Gustavsson, Tracy M Handel, Brian F Volkman

Abstract read
In one paragraph

Article in Methods in cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. NMR Studies on Protein-Ligand Interactions.International journal of molecular sciences · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Andrew B KleistDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States.
Francis PetersonDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States.
Robert C TylerDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States.
Martin GustavssonSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, CA, United States.
Tracy M HandelSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, CA, United States.
Brian F VolkmanDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States. Electronic address: bvolkman@mcw.edu.

Funding

Medical Scientist Training ProgramT32GM080202 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI BARBIERI, JOSEPH T, SALZMAN, NITA H · 2010 to 2024
$5.7M
Structural Basis for Chemokine FunctionR01AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2004 to 2019
$4.1M
Structural Basis for Chemokine FunctionR37AI058072 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI Brian F Volkman · 2020 to 2026
$2.8M
Chemokine interaction with CXCR4 and ACKR3: structure and activation mechanismsR01GM117424 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M, KUFAREVA, IRINA · 2016 to 2019
$2.2M
800 MHz NMR Spectrometer for Southeast WisconsinS10OD025000 · OD · MEDICAL COLLEGE OF WISCONSIN · PI VOLKMAN, BRIAN F · 2019 to 2019
$2.0M
Structural basis of chemokine receptor signaling in tumor progressionF30CA196040 · NCI · MEDICAL COLLEGE OF WISCONSIN · PI KLEIST, ANDREW B · 2016 to 2020
$233k
NCI NIH HHS F30 CA196040NIAID NIH HHS R01 AI058072NIAID NIH HHS R37 AI058072NIGMS NIH HHS R01 GM117424NIGMS NIH HHS T32 GM080202NIH HHS S10 OD025000
6 · The paper itself

Abstract

The past decade has witnessed remarkable progress in the determination of G protein-coupled receptor (GPCR) structures, profoundly expanding our understanding of how GPCRs recognize ligands, become activated, and interact with intracellular signaling components. In recent years, numerous studies have used solution nuclear magnetic resonance (NMR) spectroscopy to investigate GPCRs, providing fundamental insights into GPCR conformational changes, allostery, dynamics, and other facets of GPCR function are challenging to study using other structural techniques. Despite these advantages, NMR-based studies of GPCRs are few relative to the number of published structures, due in part to the challenges and limitations of NMR for the characterization of large membrane proteins. Several studies have circumvented these challenges using a variety of isotopic labeling strategies, including side chain derivatization and metabolic incorporation of NMR-active nuclei. In this chapter, we provide an overview of different isotopic labeling strategies and describe an in-depth protocol for the expression, purification, and NMR studies of the chemokine GPCR atypical chemokine receptor 3 (ACKR3) via

Indexed as

Staining and LabelingAnimalsCarbon IsotopesCell LineHumansMagnetic Resonance SpectroscopyReceptors, CXCRReceptors, G-Protein-CoupledSolutionsVitamin UACKR3 protein, humanCarbon-13Carbon IsotopesReceptors, CXCRReceptors, G-Protein-CoupledSolutionsVitamin UACKR3Atypical chemokine receptor 3Chemokine receptorGPCRG protein-coupled receptorMethionine NMRMethyl labelingNMRSolution nuclear magnetic resonance

Identifiers

PMID30616824
PMCPMC6941889

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.